The Drosophila methyl-DNA binding protein MBD2/3 interacts with the NuRD complex via p55 and MI-2
1 Research Group Epigenetics, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 580, 69120 Heidelberg, Germany
2 Adolf-Butenandt-Institut, Ludwig-Maximilians-Universität, Schillerstrasse 44, 80336 München, Germany
BMC Molecular Biology 2004, 5:20 doi:10.1186/1471-2199-5-20Published: 29 October 2004
Methyl-DNA binding proteins help to translate epigenetic information encoded by DNA methylation into covalent histone modifications. MBD2/3 is the only candidate gene in the Drosophila genome with extended homologies to mammalian MBD2 and MBD3 proteins, which represent a co-repressor and an integral component of the
The two MBD2/3 isoforms precisely cofractionated with NuRD proteins during gel filtration of extracts derived from early and late embryos. In addition, we demonstrate that MBD2/3 forms multimers, and engages in specific interactions with the p55 and MI-2 subunits of the Drosophila NuRD complex.
Our data provide novel insights into the association between Drosophila MBD2/3 and NuRD proteins. Additionally, this work provides a first analysis of the architecture of the Drosophila NuRD complex.